2QJ3

Mycobacterium tuberculosis FabD

Summary for 2QJ3

• Entry DOI: 10.2210/pdb2qj3/pdb
• Descriptor: Malonyl CoA-acyl carrier protein transacylase, NICKEL (II) ION (3 entities in total)
• Functional Keywords: malonyl-coa, fatty acid synthase, mycolic acids, transferase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 66266.36

Authors

Ghadbane, H.,Brown, A.K.,Kremer, L.,Besra, G.S.,Futterer, K. (deposition date: 2007-07-06, release date: 2007-09-04, Last modification date: 2024-10-09)

Primary citation

Ghadbane, H.,Brown, A.K.,Kremer, L.,Besra, G.S.,Futterer, K.
Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT).
Acta Crystallogr.,Sect.F, 63:831-835, 2007

PubMed Abstract: Mycobacteria display a unique and unusual cell-wall architecture, central to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan core (mAGP). The biosynthesis of mycolic acids, which form the outermost layer of the mAGP core, involves malonyl-CoA:acyl carrier protein transacylase (MCAT). This essential enzyme catalyses the transfer of malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these two-carbon units into the chain-elongation cycle of the type II fatty-acid synthase. The crystal structure of M. tuberculosis mtFabD, the mycobacterial MCAT, has been determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD.

PubMed: 17909282
DOI: 10.1107/S1744309107042455

Experimental method

X-RAY DIFFRACTION (3 Å)